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4  structures 3035  species 0  interactions 6388  sequences 96  architectures

Family: PMT (PF02366)

Summary: Dolichyl-phosphate-mannose-protein mannosyltransferase

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Dolichyl-phosphate-mannose-protein mannosyltransferase Provide feedback

This is a family of Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC: These proteins are responsible for O-linked glycosylation of proteins, they catalyse the reaction:- Dolichyl phosphate D-mannose + protein <=> dolichyl phosphate + O-D-mannosyl-protein. Also in this family is Q94891 Drosophila rotated abdomen protein which is a putative mannosyltransferase [2]. This family appears to be distantly related to PF02516 (A Bateman pers. obs.). This family also contains sequences from ArnTs (4-amino-4-deoxy-L-arabinose lipid A transferase). They catalyse the addition of 4-amino-4-deoxy-l-arabinose (l-Ara4N) to the lipid A moiety of the lipopolysaccharide [4]. This is a critical modification enabling bacteria (e.g. Escherichia coli and Salmonella typhimurium) to resist killing by antimicrobial peptides such as polymyxins [5]. Members such as O52327 are predicted to have 12 trans-membrane regions. The N-terminal portion of these proteins is hypothesised to have a conserved glycosylation activity which is shared between distantly related oligosaccharyltransferases ArnT and PglB families [4].

Literature references

  1. Gentzsch M, Tanner W; , EMBO J 1996;15:5752-5759.: The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital. PUBMED:8918452 EPMC:8918452

  2. Martin-Blanco E, Garcia-Bellido A; , Proc Natl Acad Sci U S A 1996;93:6048-6052.: Mutations in the rotated abdomen locus affect muscle development and reveal an intrinsic asymmetry in Drosophila. PUBMED:8650217 EPMC:8650217

  3. Lussier M, Gentzsch M, Sdicu AM, Bussey H, Tanner W; , J Biol Chem 1995;270:2770-2775.: Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein O-mannosyltransferase that functions in addition to the PMT1-encoded activity. PUBMED:7852348 EPMC:7852348

  4. Tavares-Carreon F, Fathy Mohamed Y, Andrade A, Valvano MA;, Glycobiology. 2016;26:286-300.: ArnT proteins that catalyze the glycosylation of lipopolysaccharide share common features with bacterial N-oligosaccharyltransferases. PUBMED:26515403 EPMC:26515403

  5. Petrou VI, Herrera CM, Schultz KM, Clarke OB, Vendome J, Tomasek D, Banerjee S, Rajashankar KR, Belcher Dufrisne M, Kloss B, Kloppmann E, Rost B, Klug CS, Trent MS, Shapiro L, Mancia F;, Science. 2016;351:608-612.: Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation. PUBMED:26912703 EPMC:26912703

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003342

The biosynthesis of disaccharides, oligosaccharides and polysaccharides involves the action of hundreds of different glycosyltransferases. These enzymes catalyse the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. A classification of glycosyltransferases using nucleotide diphospho-sugar, nucleotide monophospho-sugar and sugar phosphates ([intenz:2.4.1.-]) and related proteins into distinct sequence based families has been described [ PUBMED:9334165 ]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. The same three-dimensional fold is expected to occur within each of the families. Because 3-D structures are better conserved than sequences, several of the families defined on the basis of sequence similarities may have similar 3-D structures and therefore form 'clans'.

Dolichyl-phosphate-mannose-protein mannosyltransferase proteins EC belong to the glycosyltransferase family 39 ( CAZY ) and are responsible for O-linked glycosylation of proteins. They catalyse the reaction: Dolichyl phosphate D-mannose + protein -> dolichyl phosphate + O-D-mannosyl-protein.

The transfer of mannose to seryl and threonyl residues of secretory proteins is catalyzed by a family of protein mannosyltransferases in Saccharomyces cerevisiae coded for by seven genes (PMT1-7). Protein O-glycosylation is essential for cell wall rigidity and cell integrity and this protein modification is vital for S. cerevisiae [ PUBMED:8918452 ].

Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase proteins EC belong to the glycosyltransferase family 83 ( CAZY ). They catalyse the reaction: 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + lipid IV(A) = lipid II(A) + di-trans,octa-cis-undecaprenyl phosphate.

Gene Ontology

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Domain organisation

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Pfam Clan

This family is a member of clan GT-C (CL0111), which has the following description:

This is the GT-C clan that contains diverse glycosyltransferases that possess 8-13 predicted transmembrane segments [1].

The clan contains the following 19 members:

ALG3 Alg6_Alg8 Arabinose_trans DIE2_ALG10 DUF2079 DUF2142 DUF2723 EpsG Glucan_synthase Glyco_transf_22 GT87 Mannosyl_trans Mannosyl_trans2 PIG-U PMT PMT_2 PTPS_related STT3 YfhO


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Curation and family details

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Curation View help on the curation process

Seed source: Pfam-B_556 (release 5.2)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Bashton M , Bateman A
Number in seed: 19
Number in full: 6388
Average length of the domain: 225.00 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 33.84 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.7 22.7
Trusted cut-off 22.7 22.7
Noise cut-off 22.6 22.6
Model length: 245
Family (HMM) version: 20
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Species distribution

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Archea Archea Eukaryota Eukaryota
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the PMT domain has been found. There are 4 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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